HEADER TRANSPORT PROTEIN/IMMUNE SYSTEM 07-DEC-23 8V9D TITLE STRUCTURE OF HUMAN AQP4 WITH A PATHOGENIC AUTOANTIBODY - RAB 186 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AQUAPORIN-4; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RAB 186 HEAVY CHAIN; COMPND 7 CHAIN: I, K, M; COMPND 8 FRAGMENT: FAB; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: RAB 186 LIGHT CHAIN; COMPND 12 CHAIN: J, L, N; COMPND 13 FRAGMENT: FAB; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: AQP4; SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS AQUAPORIN, WATER-CHANNEL, TRANSPORT PROTEIN-IMMUNE SYSTEM COMPLEX, KEYWDS 2 NEUROMYELITIS OPTICA (NMO), AUTOIMMNUNE DISEASE EXPDTA ELECTRON MICROSCOPY AUTHOR M.GUPTA,N.K.KHANDELWAL,R.M.STROUD REVDAT 1 11-DEC-24 8V9D 0 JRNL AUTH M.GUPTA,N.K.KHANDELWAL,R.M.STROUD JRNL TITL HUMAN AQP4 STRUCTURE IN LIPID NANODISC USING CRYO-EM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.900 REMARK 3 NUMBER OF PARTICLES : 220335 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8V9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1000279744. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HUMAN AQP4 TETRAMER BOUND TO REMARK 245 FAB FRAGMENT OF THE PATHOGENIC REMARK 245 AUTOANTIBODY- RAB 186 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : OTHER REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, J, B, K, L, C, M, N, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -24 REMARK 465 HIS A -23 REMARK 465 HIS A -22 REMARK 465 HIS A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 ASP A -15 REMARK 465 TYR A -14 REMARK 465 LYS A -13 REMARK 465 ASP A -12 REMARK 465 ASP A -11 REMARK 465 ASP A -10 REMARK 465 ASP A -9 REMARK 465 LYS A -8 REMARK 465 LEU A -7 REMARK 465 VAL A -6 REMARK 465 PRO A -5 REMARK 465 ARG A -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 GLU A -1 REMARK 465 PHE A 0 REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 ASP A 3 REMARK 465 ARG A 4 REMARK 465 PRO A 5 REMARK 465 THR A 6 REMARK 465 ALA A 7 REMARK 465 ARG A 8 REMARK 465 ARG A 9 REMARK 465 TRP A 10 REMARK 465 GLY A 11 REMARK 465 LYS A 12 REMARK 465 CYS A 13 REMARK 465 GLY A 14 REMARK 465 PRO A 15 REMARK 465 LEU A 16 REMARK 465 CYS A 17 REMARK 465 THR A 18 REMARK 465 ARG A 19 REMARK 465 GLU A 20 REMARK 465 ASN A 21 REMARK 465 ILE A 22 REMARK 465 MET A 23 REMARK 465 VAL A 24 REMARK 465 ALA A 25 REMARK 465 PHE A 26 REMARK 465 LYS A 27 REMARK 465 GLY A 28 REMARK 465 VAL A 29 REMARK 465 TRP A 30 REMARK 465 THR A 31 REMARK 465 ASP A 255 REMARK 465 VAL A 256 REMARK 465 GLU A 257 REMARK 465 PHE A 258 REMARK 465 LYS A 259 REMARK 465 ARG A 260 REMARK 465 ARG A 261 REMARK 465 PHE A 262 REMARK 465 LYS A 263 REMARK 465 GLU A 264 REMARK 465 ALA A 265 REMARK 465 PHE A 266 REMARK 465 SER A 267 REMARK 465 LYS A 268 REMARK 465 ALA A 269 REMARK 465 ALA A 270 REMARK 465 GLN A 271 REMARK 465 GLN A 272 REMARK 465 THR A 273 REMARK 465 LYS A 274 REMARK 465 GLY A 275 REMARK 465 SER A 276 REMARK 465 TYR A 277 REMARK 465 MET A 278 REMARK 465 GLU A 279 REMARK 465 VAL A 280 REMARK 465 GLU A 281 REMARK 465 ASP A 282 REMARK 465 ASN A 283 REMARK 465 ARG A 284 REMARK 465 SER A 285 REMARK 465 GLN A 286 REMARK 465 VAL A 287 REMARK 465 GLU A 288 REMARK 465 THR A 289 REMARK 465 ASP A 290 REMARK 465 ASP A 291 REMARK 465 LEU A 292 REMARK 465 ILE A 293 REMARK 465 LEU A 294 REMARK 465 LYS A 295 REMARK 465 PRO A 296 REMARK 465 GLY A 297 REMARK 465 VAL A 298 REMARK 465 VAL A 299 REMARK 465 HIS A 300 REMARK 465 VAL A 301 REMARK 465 ILE A 302 REMARK 465 ASP A 303 REMARK 465 VAL A 304 REMARK 465 ASP A 305 REMARK 465 ARG A 306 REMARK 465 GLY A 307 REMARK 465 GLU A 308 REMARK 465 GLU A 309 REMARK 465 LYS A 310 REMARK 465 LYS A 311 REMARK 465 GLY A 312 REMARK 465 LYS A 313 REMARK 465 ASP A 314 REMARK 465 GLN A 315 REMARK 465 SER A 316 REMARK 465 GLY A 317 REMARK 465 GLU A 318 REMARK 465 VAL A 319 REMARK 465 LEU A 320 REMARK 465 SER A 321 REMARK 465 SER A 322 REMARK 465 VAL A 323 REMARK 465 SER I 0 REMARK 465 ASP I 229 REMARK 465 LYS I 230 REMARK 465 THR I 231 REMARK 465 HIS I 232 REMARK 465 MET B -24 REMARK 465 HIS B -23 REMARK 465 HIS B -22 REMARK 465 HIS B -21 REMARK 465 HIS B -20 REMARK 465 HIS B -19 REMARK 465 HIS B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 ASP B -15 REMARK 465 TYR B -14 REMARK 465 LYS B -13 REMARK 465 ASP B -12 REMARK 465 ASP B -11 REMARK 465 ASP B -10 REMARK 465 ASP B -9 REMARK 465 LYS B -8 REMARK 465 LEU B -7 REMARK 465 VAL B -6 REMARK 465 PRO B -5 REMARK 465 ARG B -4 REMARK 465 GLY B -3 REMARK 465 SER B -2 REMARK 465 GLU B -1 REMARK 465 PHE B 0 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 ASP B 3 REMARK 465 ARG B 4 REMARK 465 PRO B 5 REMARK 465 THR B 6 REMARK 465 ALA B 7 REMARK 465 ARG B 8 REMARK 465 ARG B 9 REMARK 465 TRP B 10 REMARK 465 GLY B 11 REMARK 465 LYS B 12 REMARK 465 CYS B 13 REMARK 465 GLY B 14 REMARK 465 PRO B 15 REMARK 465 LEU B 16 REMARK 465 CYS B 17 REMARK 465 THR B 18 REMARK 465 ARG B 19 REMARK 465 GLU B 20 REMARK 465 ASN B 21 REMARK 465 ILE B 22 REMARK 465 MET B 23 REMARK 465 VAL B 24 REMARK 465 ALA B 25 REMARK 465 PHE B 26 REMARK 465 LYS B 27 REMARK 465 GLY B 28 REMARK 465 VAL B 29 REMARK 465 TRP B 30 REMARK 465 THR B 31 REMARK 465 ASP B 255 REMARK 465 VAL B 256 REMARK 465 GLU B 257 REMARK 465 PHE B 258 REMARK 465 LYS B 259 REMARK 465 ARG B 260 REMARK 465 ARG B 261 REMARK 465 PHE B 262 REMARK 465 LYS B 263 REMARK 465 GLU B 264 REMARK 465 ALA B 265 REMARK 465 PHE B 266 REMARK 465 SER B 267 REMARK 465 LYS B 268 REMARK 465 ALA B 269 REMARK 465 ALA B 270 REMARK 465 GLN B 271 REMARK 465 GLN B 272 REMARK 465 THR B 273 REMARK 465 LYS B 274 REMARK 465 GLY B 275 REMARK 465 SER B 276 REMARK 465 TYR B 277 REMARK 465 MET B 278 REMARK 465 GLU B 279 REMARK 465 VAL B 280 REMARK 465 GLU B 281 REMARK 465 ASP B 282 REMARK 465 ASN B 283 REMARK 465 ARG B 284 REMARK 465 SER B 285 REMARK 465 GLN B 286 REMARK 465 VAL B 287 REMARK 465 GLU B 288 REMARK 465 THR B 289 REMARK 465 ASP B 290 REMARK 465 ASP B 291 REMARK 465 LEU B 292 REMARK 465 ILE B 293 REMARK 465 LEU B 294 REMARK 465 LYS B 295 REMARK 465 PRO B 296 REMARK 465 GLY B 297 REMARK 465 VAL B 298 REMARK 465 VAL B 299 REMARK 465 HIS B 300 REMARK 465 VAL B 301 REMARK 465 ILE B 302 REMARK 465 ASP B 303 REMARK 465 VAL B 304 REMARK 465 ASP B 305 REMARK 465 ARG B 306 REMARK 465 GLY B 307 REMARK 465 GLU B 308 REMARK 465 GLU B 309 REMARK 465 LYS B 310 REMARK 465 LYS B 311 REMARK 465 GLY B 312 REMARK 465 LYS B 313 REMARK 465 ASP B 314 REMARK 465 GLN B 315 REMARK 465 SER B 316 REMARK 465 GLY B 317 REMARK 465 GLU B 318 REMARK 465 VAL B 319 REMARK 465 LEU B 320 REMARK 465 SER B 321 REMARK 465 SER B 322 REMARK 465 VAL B 323 REMARK 465 SER K 0 REMARK 465 ASP K 229 REMARK 465 LYS K 230 REMARK 465 THR K 231 REMARK 465 HIS K 232 REMARK 465 MET C -24 REMARK 465 HIS C -23 REMARK 465 HIS C -22 REMARK 465 HIS C -21 REMARK 465 HIS C -20 REMARK 465 HIS C -19 REMARK 465 HIS C -18 REMARK 465 HIS C -17 REMARK 465 HIS C -16 REMARK 465 ASP C -15 REMARK 465 TYR C -14 REMARK 465 LYS C -13 REMARK 465 ASP C -12 REMARK 465 ASP C -11 REMARK 465 ASP C -10 REMARK 465 ASP C -9 REMARK 465 LYS C -8 REMARK 465 LEU C -7 REMARK 465 VAL C -6 REMARK 465 PRO C -5 REMARK 465 ARG C -4 REMARK 465 GLY C -3 REMARK 465 SER C -2 REMARK 465 GLU C -1 REMARK 465 PHE C 0 REMARK 465 MET C 1 REMARK 465 SER C 2 REMARK 465 ASP C 3 REMARK 465 ARG C 4 REMARK 465 PRO C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 ARG C 8 REMARK 465 ARG C 9 REMARK 465 TRP C 10 REMARK 465 GLY C 11 REMARK 465 LYS C 12 REMARK 465 CYS C 13 REMARK 465 GLY C 14 REMARK 465 PRO C 15 REMARK 465 LEU C 16 REMARK 465 CYS C 17 REMARK 465 THR C 18 REMARK 465 ARG C 19 REMARK 465 GLU C 20 REMARK 465 ASN C 21 REMARK 465 ILE C 22 REMARK 465 MET C 23 REMARK 465 VAL C 24 REMARK 465 ALA C 25 REMARK 465 PHE C 26 REMARK 465 LYS C 27 REMARK 465 GLY C 28 REMARK 465 VAL C 29 REMARK 465 TRP C 30 REMARK 465 THR C 31 REMARK 465 ASP C 255 REMARK 465 VAL C 256 REMARK 465 GLU C 257 REMARK 465 PHE C 258 REMARK 465 LYS C 259 REMARK 465 ARG C 260 REMARK 465 ARG C 261 REMARK 465 PHE C 262 REMARK 465 LYS C 263 REMARK 465 GLU C 264 REMARK 465 ALA C 265 REMARK 465 PHE C 266 REMARK 465 SER C 267 REMARK 465 LYS C 268 REMARK 465 ALA C 269 REMARK 465 ALA C 270 REMARK 465 GLN C 271 REMARK 465 GLN C 272 REMARK 465 THR C 273 REMARK 465 LYS C 274 REMARK 465 GLY C 275 REMARK 465 SER C 276 REMARK 465 TYR C 277 REMARK 465 MET C 278 REMARK 465 GLU C 279 REMARK 465 VAL C 280 REMARK 465 GLU C 281 REMARK 465 ASP C 282 REMARK 465 ASN C 283 REMARK 465 ARG C 284 REMARK 465 SER C 285 REMARK 465 GLN C 286 REMARK 465 VAL C 287 REMARK 465 GLU C 288 REMARK 465 THR C 289 REMARK 465 ASP C 290 REMARK 465 ASP C 291 REMARK 465 LEU C 292 REMARK 465 ILE C 293 REMARK 465 LEU C 294 REMARK 465 LYS C 295 REMARK 465 PRO C 296 REMARK 465 GLY C 297 REMARK 465 VAL C 298 REMARK 465 VAL C 299 REMARK 465 HIS C 300 REMARK 465 VAL C 301 REMARK 465 ILE C 302 REMARK 465 ASP C 303 REMARK 465 VAL C 304 REMARK 465 ASP C 305 REMARK 465 ARG C 306 REMARK 465 GLY C 307 REMARK 465 GLU C 308 REMARK 465 GLU C 309 REMARK 465 LYS C 310 REMARK 465 LYS C 311 REMARK 465 GLY C 312 REMARK 465 LYS C 313 REMARK 465 ASP C 314 REMARK 465 GLN C 315 REMARK 465 SER C 316 REMARK 465 GLY C 317 REMARK 465 GLU C 318 REMARK 465 VAL C 319 REMARK 465 LEU C 320 REMARK 465 SER C 321 REMARK 465 SER C 322 REMARK 465 VAL C 323 REMARK 465 SER M 0 REMARK 465 ASP M 229 REMARK 465 LYS M 230 REMARK 465 THR M 231 REMARK 465 HIS M 232 REMARK 465 MET D -24 REMARK 465 HIS D -23 REMARK 465 HIS D -22 REMARK 465 HIS D -21 REMARK 465 HIS D -20 REMARK 465 HIS D -19 REMARK 465 HIS D -18 REMARK 465 HIS D -17 REMARK 465 HIS D -16 REMARK 465 ASP D -15 REMARK 465 TYR D -14 REMARK 465 LYS D -13 REMARK 465 ASP D -12 REMARK 465 ASP D -11 REMARK 465 ASP D -10 REMARK 465 ASP D -9 REMARK 465 LYS D -8 REMARK 465 LEU D -7 REMARK 465 VAL D -6 REMARK 465 PRO D -5 REMARK 465 ARG D -4 REMARK 465 GLY D -3 REMARK 465 SER D -2 REMARK 465 GLU D -1 REMARK 465 PHE D 0 REMARK 465 MET D 1 REMARK 465 SER D 2 REMARK 465 ASP D 3 REMARK 465 ARG D 4 REMARK 465 PRO D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 ARG D 8 REMARK 465 ARG D 9 REMARK 465 TRP D 10 REMARK 465 GLY D 11 REMARK 465 LYS D 12 REMARK 465 CYS D 13 REMARK 465 GLY D 14 REMARK 465 PRO D 15 REMARK 465 LEU D 16 REMARK 465 CYS D 17 REMARK 465 THR D 18 REMARK 465 ARG D 19 REMARK 465 GLU D 20 REMARK 465 ASN D 21 REMARK 465 ILE D 22 REMARK 465 MET D 23 REMARK 465 VAL D 24 REMARK 465 ALA D 25 REMARK 465 PHE D 26 REMARK 465 LYS D 27 REMARK 465 GLY D 28 REMARK 465 VAL D 29 REMARK 465 TRP D 30 REMARK 465 THR D 31 REMARK 465 ASP D 255 REMARK 465 VAL D 256 REMARK 465 GLU D 257 REMARK 465 PHE D 258 REMARK 465 LYS D 259 REMARK 465 ARG D 260 REMARK 465 ARG D 261 REMARK 465 PHE D 262 REMARK 465 LYS D 263 REMARK 465 GLU D 264 REMARK 465 ALA D 265 REMARK 465 PHE D 266 REMARK 465 SER D 267 REMARK 465 LYS D 268 REMARK 465 ALA D 269 REMARK 465 ALA D 270 REMARK 465 GLN D 271 REMARK 465 GLN D 272 REMARK 465 THR D 273 REMARK 465 LYS D 274 REMARK 465 GLY D 275 REMARK 465 SER D 276 REMARK 465 TYR D 277 REMARK 465 MET D 278 REMARK 465 GLU D 279 REMARK 465 VAL D 280 REMARK 465 GLU D 281 REMARK 465 ASP D 282 REMARK 465 ASN D 283 REMARK 465 ARG D 284 REMARK 465 SER D 285 REMARK 465 GLN D 286 REMARK 465 VAL D 287 REMARK 465 GLU D 288 REMARK 465 THR D 289 REMARK 465 ASP D 290 REMARK 465 ASP D 291 REMARK 465 LEU D 292 REMARK 465 ILE D 293 REMARK 465 LEU D 294 REMARK 465 LYS D 295 REMARK 465 PRO D 296 REMARK 465 GLY D 297 REMARK 465 VAL D 298 REMARK 465 VAL D 299 REMARK 465 HIS D 300 REMARK 465 VAL D 301 REMARK 465 ILE D 302 REMARK 465 ASP D 303 REMARK 465 VAL D 304 REMARK 465 ASP D 305 REMARK 465 ARG D 306 REMARK 465 GLY D 307 REMARK 465 GLU D 308 REMARK 465 GLU D 309 REMARK 465 LYS D 310 REMARK 465 LYS D 311 REMARK 465 GLY D 312 REMARK 465 LYS D 313 REMARK 465 ASP D 314 REMARK 465 GLN D 315 REMARK 465 SER D 316 REMARK 465 GLY D 317 REMARK 465 GLU D 318 REMARK 465 VAL D 319 REMARK 465 LEU D 320 REMARK 465 SER D 321 REMARK 465 SER D 322 REMARK 465 VAL D 323 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS I 222 CG CD CE NZ REMARK 470 LYS K 222 CG CD CE NZ REMARK 470 LYS M 222 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLU L 196 OG1 THR L 207 1.94 REMARK 500 ND2 ASN A 226 O HOH A 401 1.97 REMARK 500 OD2 ASP I 74 NZ LYS I 77 2.17 REMARK 500 O TYR D 134 O HOH D 401 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 97 119.56 -163.03 REMARK 500 VAL A 251 -52.57 -121.09 REMARK 500 SER I 15 3.35 82.05 REMARK 500 ILE I 50 -61.46 -121.97 REMARK 500 PHE I 111 173.47 -56.71 REMARK 500 ALA J 52 -6.04 75.43 REMARK 500 SER K 15 3.37 81.79 REMARK 500 ILE K 50 -59.96 -121.67 REMARK 500 PHE K 111 172.68 -56.47 REMARK 500 ALA L 52 -6.26 75.36 REMARK 500 VAL C 251 -50.93 -121.25 REMARK 500 SER M 15 2.31 81.97 REMARK 500 ILE M 50 -61.77 -122.26 REMARK 500 PHE M 111 172.07 -56.94 REMARK 500 ALA N 52 -6.71 75.73 REMARK 500 ASN D 97 119.49 -166.67 REMARK 500 VAL D 251 -53.51 -123.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43071 RELATED DB: EMDB REMARK 900 STRUCTURE OF HUMAN AQP4 WITH A PATHOGENIC AUTOANTIBODY- RAB 186 DBREF 8V9D A 1 323 UNP P55087 AQP4_HUMAN 1 323 DBREF 8V9D I 0 232 PDB 8V9D 8V9D 0 232 DBREF 8V9D J 1 215 PDB 8V9D 8V9D 1 215 DBREF 8V9D B 1 323 UNP P55087 AQP4_HUMAN 1 323 DBREF 8V9D K 0 232 PDB 8V9D 8V9D 0 232 DBREF 8V9D L 1 215 PDB 8V9D 8V9D 1 215 DBREF 8V9D C 1 323 UNP P55087 AQP4_HUMAN 1 323 DBREF 8V9D M 0 232 PDB 8V9D 8V9D 0 232 DBREF 8V9D N 1 215 PDB 8V9D 8V9D 1 215 DBREF 8V9D D 1 323 UNP P55087 AQP4_HUMAN 1 323 SEQADV 8V9D MET A -24 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -23 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -22 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -21 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -20 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -19 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -18 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -17 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS A -16 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP A -15 UNP P55087 EXPRESSION TAG SEQADV 8V9D TYR A -14 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS A -13 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP A -12 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP A -11 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP A -10 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP A -9 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS A -8 UNP P55087 EXPRESSION TAG SEQADV 8V9D LEU A -7 UNP P55087 EXPRESSION TAG SEQADV 8V9D VAL A -6 UNP P55087 EXPRESSION TAG SEQADV 8V9D PRO A -5 UNP P55087 EXPRESSION TAG SEQADV 8V9D ARG A -4 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLY A -3 UNP P55087 EXPRESSION TAG SEQADV 8V9D SER A -2 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLU A -1 UNP P55087 EXPRESSION TAG SEQADV 8V9D PHE A 0 UNP P55087 EXPRESSION TAG SEQADV 8V9D MET B -24 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -23 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -22 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -21 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -20 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -19 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -18 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -17 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS B -16 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP B -15 UNP P55087 EXPRESSION TAG SEQADV 8V9D TYR B -14 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS B -13 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP B -12 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP B -11 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP B -10 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP B -9 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS B -8 UNP P55087 EXPRESSION TAG SEQADV 8V9D LEU B -7 UNP P55087 EXPRESSION TAG SEQADV 8V9D VAL B -6 UNP P55087 EXPRESSION TAG SEQADV 8V9D PRO B -5 UNP P55087 EXPRESSION TAG SEQADV 8V9D ARG B -4 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLY B -3 UNP P55087 EXPRESSION TAG SEQADV 8V9D SER B -2 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLU B -1 UNP P55087 EXPRESSION TAG SEQADV 8V9D PHE B 0 UNP P55087 EXPRESSION TAG SEQADV 8V9D MET C -24 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -23 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -22 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -21 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -20 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -19 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -18 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -17 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS C -16 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP C -15 UNP P55087 EXPRESSION TAG SEQADV 8V9D TYR C -14 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS C -13 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP C -12 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP C -11 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP C -10 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP C -9 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS C -8 UNP P55087 EXPRESSION TAG SEQADV 8V9D LEU C -7 UNP P55087 EXPRESSION TAG SEQADV 8V9D VAL C -6 UNP P55087 EXPRESSION TAG SEQADV 8V9D PRO C -5 UNP P55087 EXPRESSION TAG SEQADV 8V9D ARG C -4 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLY C -3 UNP P55087 EXPRESSION TAG SEQADV 8V9D SER C -2 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLU C -1 UNP P55087 EXPRESSION TAG SEQADV 8V9D PHE C 0 UNP P55087 EXPRESSION TAG SEQADV 8V9D MET D -24 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -23 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -22 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -21 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -20 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -19 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -18 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -17 UNP P55087 EXPRESSION TAG SEQADV 8V9D HIS D -16 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP D -15 UNP P55087 EXPRESSION TAG SEQADV 8V9D TYR D -14 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS D -13 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP D -12 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP D -11 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP D -10 UNP P55087 EXPRESSION TAG SEQADV 8V9D ASP D -9 UNP P55087 EXPRESSION TAG SEQADV 8V9D LYS D -8 UNP P55087 EXPRESSION TAG SEQADV 8V9D LEU D -7 UNP P55087 EXPRESSION TAG SEQADV 8V9D VAL D -6 UNP P55087 EXPRESSION TAG SEQADV 8V9D PRO D -5 UNP P55087 EXPRESSION TAG SEQADV 8V9D ARG D -4 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLY D -3 UNP P55087 EXPRESSION TAG SEQADV 8V9D SER D -2 UNP P55087 EXPRESSION TAG SEQADV 8V9D GLU D -1 UNP P55087 EXPRESSION TAG SEQADV 8V9D PHE D 0 UNP P55087 EXPRESSION TAG SEQRES 1 A 348 MET HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP SEQRES 2 A 348 ASP ASP ASP LYS LEU VAL PRO ARG GLY SER GLU PHE MET SEQRES 3 A 348 SER ASP ARG PRO THR ALA ARG ARG TRP GLY LYS CYS GLY SEQRES 4 A 348 PRO LEU CYS THR ARG GLU ASN ILE MET VAL ALA PHE LYS SEQRES 5 A 348 GLY VAL TRP THR GLN ALA PHE TRP LYS ALA VAL THR ALA SEQRES 6 A 348 GLU PHE LEU ALA MET LEU ILE PHE VAL LEU LEU SER LEU SEQRES 7 A 348 GLY SER THR ILE ASN TRP GLY GLY THR GLU LYS PRO LEU SEQRES 8 A 348 PRO VAL ASP MET VAL LEU ILE SER LEU CYS PHE GLY LEU SEQRES 9 A 348 SER ILE ALA THR MET VAL GLN CYS PHE GLY HIS ILE SER SEQRES 10 A 348 GLY GLY HIS ILE ASN PRO ALA VAL THR VAL ALA MET VAL SEQRES 11 A 348 CYS THR ARG LYS ILE SER ILE ALA LYS SER VAL PHE TYR SEQRES 12 A 348 ILE ALA ALA GLN CYS LEU GLY ALA ILE ILE GLY ALA GLY SEQRES 13 A 348 ILE LEU TYR LEU VAL THR PRO PRO SER VAL VAL GLY GLY SEQRES 14 A 348 LEU GLY VAL THR MET VAL HIS GLY ASN LEU THR ALA GLY SEQRES 15 A 348 HIS GLY LEU LEU VAL GLU LEU ILE ILE THR PHE GLN LEU SEQRES 16 A 348 VAL PHE THR ILE PHE ALA SER CYS ASP SER LYS ARG THR SEQRES 17 A 348 ASP VAL THR GLY SER ILE ALA LEU ALA ILE GLY PHE SER SEQRES 18 A 348 VAL ALA ILE GLY HIS LEU PHE ALA ILE ASN TYR THR GLY SEQRES 19 A 348 ALA SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL SEQRES 20 A 348 ILE MET GLY ASN TRP GLU ASN HIS TRP ILE TYR TRP VAL SEQRES 21 A 348 GLY PRO ILE ILE GLY ALA VAL LEU ALA GLY GLY LEU TYR SEQRES 22 A 348 GLU TYR VAL PHE CYS PRO ASP VAL GLU PHE LYS ARG ARG SEQRES 23 A 348 PHE LYS GLU ALA PHE SER LYS ALA ALA GLN GLN THR LYS SEQRES 24 A 348 GLY SER TYR MET GLU VAL GLU ASP ASN ARG SER GLN VAL SEQRES 25 A 348 GLU THR ASP ASP LEU ILE LEU LYS PRO GLY VAL VAL HIS SEQRES 26 A 348 VAL ILE ASP VAL ASP ARG GLY GLU GLU LYS LYS GLY LYS SEQRES 27 A 348 ASP GLN SER GLY GLU VAL LEU SER SER VAL SEQRES 1 I 233 SER GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL SEQRES 2 I 233 LYS PRO SER GLN THR LEU PRO LEU THR CYS THR VAL SER SEQRES 3 I 233 GLY GLY TYR ILE SER SER GLY SER HIS GLN TRP GLY TRP SEQRES 4 I 233 ILE ARG GLN PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 I 233 ARG ILE TYR THR SER GLY SER THR ASN TYR ASN PRO SER SEQRES 6 I 233 LEU LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS SEQRES 7 I 233 ASN GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA SEQRES 8 I 233 ASP THR ALA VAL TYR TYR CYS ALA ARG VAL ASN TYR ASP SEQRES 9 I 233 LEU LEU THR GLY ARG ALA ASN PHE PHE ASP PRO TRP GLY SEQRES 10 I 233 GLN GLY THR PRO VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 I 233 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 I 233 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 I 233 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 I 233 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 I 233 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 I 233 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 I 233 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 I 233 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 J 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 J 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 215 GLN SER VAL SER SER ARG SER VAL ALA TRP TYR GLN GLN SEQRES 4 J 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 J 215 SER ASN ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 J 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 J 215 LEU GLU PRO GLU ASP PHE VAL VAL PHE TYR CYS GLN GLN SEQRES 8 J 215 TYR GLY SER SER PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 J 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 J 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 J 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 J 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 J 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 J 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 J 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 J 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 J 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 348 MET HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP SEQRES 2 B 348 ASP ASP ASP LYS LEU VAL PRO ARG GLY SER GLU PHE MET SEQRES 3 B 348 SER ASP ARG PRO THR ALA ARG ARG TRP GLY LYS CYS GLY SEQRES 4 B 348 PRO LEU CYS THR ARG GLU ASN ILE MET VAL ALA PHE LYS SEQRES 5 B 348 GLY VAL TRP THR GLN ALA PHE TRP LYS ALA VAL THR ALA SEQRES 6 B 348 GLU PHE LEU ALA MET LEU ILE PHE VAL LEU LEU SER LEU SEQRES 7 B 348 GLY SER THR ILE ASN TRP GLY GLY THR GLU LYS PRO LEU SEQRES 8 B 348 PRO VAL ASP MET VAL LEU ILE SER LEU CYS PHE GLY LEU SEQRES 9 B 348 SER ILE ALA THR MET VAL GLN CYS PHE GLY HIS ILE SER SEQRES 10 B 348 GLY GLY HIS ILE ASN PRO ALA VAL THR VAL ALA MET VAL SEQRES 11 B 348 CYS THR ARG LYS ILE SER ILE ALA LYS SER VAL PHE TYR SEQRES 12 B 348 ILE ALA ALA GLN CYS LEU GLY ALA ILE ILE GLY ALA GLY SEQRES 13 B 348 ILE LEU TYR LEU VAL THR PRO PRO SER VAL VAL GLY GLY SEQRES 14 B 348 LEU GLY VAL THR MET VAL HIS GLY ASN LEU THR ALA GLY SEQRES 15 B 348 HIS GLY LEU LEU VAL GLU LEU ILE ILE THR PHE GLN LEU SEQRES 16 B 348 VAL PHE THR ILE PHE ALA SER CYS ASP SER LYS ARG THR SEQRES 17 B 348 ASP VAL THR GLY SER ILE ALA LEU ALA ILE GLY PHE SER SEQRES 18 B 348 VAL ALA ILE GLY HIS LEU PHE ALA ILE ASN TYR THR GLY SEQRES 19 B 348 ALA SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL SEQRES 20 B 348 ILE MET GLY ASN TRP GLU ASN HIS TRP ILE TYR TRP VAL SEQRES 21 B 348 GLY PRO ILE ILE GLY ALA VAL LEU ALA GLY GLY LEU TYR SEQRES 22 B 348 GLU TYR VAL PHE CYS PRO ASP VAL GLU PHE LYS ARG ARG SEQRES 23 B 348 PHE LYS GLU ALA PHE SER LYS ALA ALA GLN GLN THR LYS SEQRES 24 B 348 GLY SER TYR MET GLU VAL GLU ASP ASN ARG SER GLN VAL SEQRES 25 B 348 GLU THR ASP ASP LEU ILE LEU LYS PRO GLY VAL VAL HIS SEQRES 26 B 348 VAL ILE ASP VAL ASP ARG GLY GLU GLU LYS LYS GLY LYS SEQRES 27 B 348 ASP GLN SER GLY GLU VAL LEU SER SER VAL SEQRES 1 K 233 SER GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL SEQRES 2 K 233 LYS PRO SER GLN THR LEU PRO LEU THR CYS THR VAL SER SEQRES 3 K 233 GLY GLY TYR ILE SER SER GLY SER HIS GLN TRP GLY TRP SEQRES 4 K 233 ILE ARG GLN PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 K 233 ARG ILE TYR THR SER GLY SER THR ASN TYR ASN PRO SER SEQRES 6 K 233 LEU LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS SEQRES 7 K 233 ASN GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA SEQRES 8 K 233 ASP THR ALA VAL TYR TYR CYS ALA ARG VAL ASN TYR ASP SEQRES 9 K 233 LEU LEU THR GLY ARG ALA ASN PHE PHE ASP PRO TRP GLY SEQRES 10 K 233 GLN GLY THR PRO VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 K 233 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 K 233 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 K 233 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 K 233 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 K 233 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 K 233 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 K 233 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 K 233 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER ARG SER VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 215 SER ASN ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 215 LEU GLU PRO GLU ASP PHE VAL VAL PHE TYR CYS GLN GLN SEQRES 8 L 215 TYR GLY SER SER PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 348 MET HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP SEQRES 2 C 348 ASP ASP ASP LYS LEU VAL PRO ARG GLY SER GLU PHE MET SEQRES 3 C 348 SER ASP ARG PRO THR ALA ARG ARG TRP GLY LYS CYS GLY SEQRES 4 C 348 PRO LEU CYS THR ARG GLU ASN ILE MET VAL ALA PHE LYS SEQRES 5 C 348 GLY VAL TRP THR GLN ALA PHE TRP LYS ALA VAL THR ALA SEQRES 6 C 348 GLU PHE LEU ALA MET LEU ILE PHE VAL LEU LEU SER LEU SEQRES 7 C 348 GLY SER THR ILE ASN TRP GLY GLY THR GLU LYS PRO LEU SEQRES 8 C 348 PRO VAL ASP MET VAL LEU ILE SER LEU CYS PHE GLY LEU SEQRES 9 C 348 SER ILE ALA THR MET VAL GLN CYS PHE GLY HIS ILE SER SEQRES 10 C 348 GLY GLY HIS ILE ASN PRO ALA VAL THR VAL ALA MET VAL SEQRES 11 C 348 CYS THR ARG LYS ILE SER ILE ALA LYS SER VAL PHE TYR SEQRES 12 C 348 ILE ALA ALA GLN CYS LEU GLY ALA ILE ILE GLY ALA GLY SEQRES 13 C 348 ILE LEU TYR LEU VAL THR PRO PRO SER VAL VAL GLY GLY SEQRES 14 C 348 LEU GLY VAL THR MET VAL HIS GLY ASN LEU THR ALA GLY SEQRES 15 C 348 HIS GLY LEU LEU VAL GLU LEU ILE ILE THR PHE GLN LEU SEQRES 16 C 348 VAL PHE THR ILE PHE ALA SER CYS ASP SER LYS ARG THR SEQRES 17 C 348 ASP VAL THR GLY SER ILE ALA LEU ALA ILE GLY PHE SER SEQRES 18 C 348 VAL ALA ILE GLY HIS LEU PHE ALA ILE ASN TYR THR GLY SEQRES 19 C 348 ALA SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL SEQRES 20 C 348 ILE MET GLY ASN TRP GLU ASN HIS TRP ILE TYR TRP VAL SEQRES 21 C 348 GLY PRO ILE ILE GLY ALA VAL LEU ALA GLY GLY LEU TYR SEQRES 22 C 348 GLU TYR VAL PHE CYS PRO ASP VAL GLU PHE LYS ARG ARG SEQRES 23 C 348 PHE LYS GLU ALA PHE SER LYS ALA ALA GLN GLN THR LYS SEQRES 24 C 348 GLY SER TYR MET GLU VAL GLU ASP ASN ARG SER GLN VAL SEQRES 25 C 348 GLU THR ASP ASP LEU ILE LEU LYS PRO GLY VAL VAL HIS SEQRES 26 C 348 VAL ILE ASP VAL ASP ARG GLY GLU GLU LYS LYS GLY LYS SEQRES 27 C 348 ASP GLN SER GLY GLU VAL LEU SER SER VAL SEQRES 1 M 233 SER GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL SEQRES 2 M 233 LYS PRO SER GLN THR LEU PRO LEU THR CYS THR VAL SER SEQRES 3 M 233 GLY GLY TYR ILE SER SER GLY SER HIS GLN TRP GLY TRP SEQRES 4 M 233 ILE ARG GLN PRO ALA GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 M 233 ARG ILE TYR THR SER GLY SER THR ASN TYR ASN PRO SER SEQRES 6 M 233 LEU LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS SEQRES 7 M 233 ASN GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA SEQRES 8 M 233 ASP THR ALA VAL TYR TYR CYS ALA ARG VAL ASN TYR ASP SEQRES 9 M 233 LEU LEU THR GLY ARG ALA ASN PHE PHE ASP PRO TRP GLY SEQRES 10 M 233 GLN GLY THR PRO VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 M 233 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 M 233 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 M 233 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 M 233 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 M 233 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 M 233 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 M 233 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 M 233 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 1 N 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 N 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 N 215 GLN SER VAL SER SER ARG SER VAL ALA TRP TYR GLN GLN SEQRES 4 N 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 N 215 SER ASN ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 N 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 N 215 LEU GLU PRO GLU ASP PHE VAL VAL PHE TYR CYS GLN GLN SEQRES 8 N 215 TYR GLY SER SER PRO LEU THR PHE GLY GLY GLY THR LYS SEQRES 9 N 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 N 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 N 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 N 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 N 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 N 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 N 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 N 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 N 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 348 MET HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP SEQRES 2 D 348 ASP ASP ASP LYS LEU VAL PRO ARG GLY SER GLU PHE MET SEQRES 3 D 348 SER ASP ARG PRO THR ALA ARG ARG TRP GLY LYS CYS GLY SEQRES 4 D 348 PRO LEU CYS THR ARG GLU ASN ILE MET VAL ALA PHE LYS SEQRES 5 D 348 GLY VAL TRP THR GLN ALA PHE TRP LYS ALA VAL THR ALA SEQRES 6 D 348 GLU PHE LEU ALA MET LEU ILE PHE VAL LEU LEU SER LEU SEQRES 7 D 348 GLY SER THR ILE ASN TRP GLY GLY THR GLU LYS PRO LEU SEQRES 8 D 348 PRO VAL ASP MET VAL LEU ILE SER LEU CYS PHE GLY LEU SEQRES 9 D 348 SER ILE ALA THR MET VAL GLN CYS PHE GLY HIS ILE SER SEQRES 10 D 348 GLY GLY HIS ILE ASN PRO ALA VAL THR VAL ALA MET VAL SEQRES 11 D 348 CYS THR ARG LYS ILE SER ILE ALA LYS SER VAL PHE TYR SEQRES 12 D 348 ILE ALA ALA GLN CYS LEU GLY ALA ILE ILE GLY ALA GLY SEQRES 13 D 348 ILE LEU TYR LEU VAL THR PRO PRO SER VAL VAL GLY GLY SEQRES 14 D 348 LEU GLY VAL THR MET VAL HIS GLY ASN LEU THR ALA GLY SEQRES 15 D 348 HIS GLY LEU LEU VAL GLU LEU ILE ILE THR PHE GLN LEU SEQRES 16 D 348 VAL PHE THR ILE PHE ALA SER CYS ASP SER LYS ARG THR SEQRES 17 D 348 ASP VAL THR GLY SER ILE ALA LEU ALA ILE GLY PHE SER SEQRES 18 D 348 VAL ALA ILE GLY HIS LEU PHE ALA ILE ASN TYR THR GLY SEQRES 19 D 348 ALA SER MET ASN PRO ALA ARG SER PHE GLY PRO ALA VAL SEQRES 20 D 348 ILE MET GLY ASN TRP GLU ASN HIS TRP ILE TYR TRP VAL SEQRES 21 D 348 GLY PRO ILE ILE GLY ALA VAL LEU ALA GLY GLY LEU TYR SEQRES 22 D 348 GLU TYR VAL PHE CYS PRO ASP VAL GLU PHE LYS ARG ARG SEQRES 23 D 348 PHE LYS GLU ALA PHE SER LYS ALA ALA GLN GLN THR LYS SEQRES 24 D 348 GLY SER TYR MET GLU VAL GLU ASP ASN ARG SER GLN VAL SEQRES 25 D 348 GLU THR ASP ASP LEU ILE LEU LYS PRO GLY VAL VAL HIS SEQRES 26 D 348 VAL ILE ASP VAL ASP ARG GLY GLU GLU LYS LYS GLY LYS SEQRES 27 D 348 ASP GLN SER GLY GLU VAL LEU SER SER VAL FORMUL 11 HOH *80(H2 O) HELIX 1 AA1 GLN A 32 SER A 55 1 24 HELIX 2 AA2 ASP A 69 GLY A 93 1 25 HELIX 3 AA3 ASN A 97 THR A 107 1 11 HELIX 4 AA4 SER A 111 THR A 137 1 27 HELIX 5 AA5 THR A 155 CYS A 178 1 24 HELIX 6 AA6 SER A 188 ILE A 205 1 18 HELIX 7 AA7 ASN A 213 GLY A 225 1 13 HELIX 8 AA8 TRP A 231 VAL A 251 1 21 HELIX 9 AA9 THR I 88 THR I 92 5 5 HELIX 10 AB1 SER I 139 LYS I 141 5 3 HELIX 11 AB2 SER I 168 ALA I 170 5 3 HELIX 12 AB3 SER I 199 LEU I 201 5 3 HELIX 13 AB4 VAL J 29 ARG J 32 5 4 HELIX 14 AB5 GLU J 80 PHE J 84 5 5 HELIX 15 AB6 SER J 122 SER J 128 1 7 HELIX 16 AB7 LYS J 184 HIS J 190 1 7 HELIX 17 AB8 ALA B 33 SER B 55 1 23 HELIX 18 AB9 ASP B 69 GLY B 93 1 25 HELIX 19 AC1 ASN B 97 THR B 107 1 11 HELIX 20 AC2 SER B 111 THR B 137 1 27 HELIX 21 AC3 THR B 155 CYS B 178 1 24 HELIX 22 AC4 SER B 188 ILE B 205 1 18 HELIX 23 AC5 ASN B 213 GLY B 225 1 13 HELIX 24 AC6 TRP B 231 VAL B 251 1 21 HELIX 25 AC7 PRO K 63 LYS K 66 5 4 HELIX 26 AC8 THR K 88 THR K 92 5 5 HELIX 27 AC9 SER K 139 LYS K 141 5 3 HELIX 28 AD1 SER K 168 ALA K 170 5 3 HELIX 29 AD2 SER K 199 LEU K 201 5 3 HELIX 30 AD3 VAL L 29 ARG L 32 5 4 HELIX 31 AD4 GLU L 80 PHE L 84 5 5 HELIX 32 AD5 SER L 122 SER L 128 1 7 HELIX 33 AD6 LYS L 184 HIS L 190 1 7 HELIX 34 AD7 ALA C 33 SER C 55 1 23 HELIX 35 AD8 ASP C 69 GLY C 93 1 25 HELIX 36 AD9 ASN C 97 THR C 107 1 11 HELIX 37 AE1 SER C 111 THR C 137 1 27 HELIX 38 AE2 THR C 155 CYS C 178 1 24 HELIX 39 AE3 SER C 188 ILE C 205 1 18 HELIX 40 AE4 ASN C 213 GLY C 225 1 13 HELIX 41 AE5 TRP C 231 VAL C 251 1 21 HELIX 42 AE6 THR M 88 THR M 92 5 5 HELIX 43 AE7 SER M 139 LYS M 141 5 3 HELIX 44 AE8 SER M 168 ALA M 170 5 3 HELIX 45 AE9 SER M 199 LEU M 201 5 3 HELIX 46 AF1 VAL N 29 ARG N 32 5 4 HELIX 47 AF2 GLU N 80 PHE N 84 5 5 HELIX 48 AF3 SER N 122 SER N 128 1 7 HELIX 49 AF4 LYS N 184 HIS N 190 1 7 HELIX 50 AF5 ALA D 33 SER D 55 1 23 HELIX 51 AF6 ASP D 69 GLY D 93 1 25 HELIX 52 AF7 ASN D 97 THR D 107 1 11 HELIX 53 AF8 SER D 111 THR D 137 1 27 HELIX 54 AF9 THR D 155 CYS D 178 1 24 HELIX 55 AG1 SER D 188 ILE D 205 1 18 HELIX 56 AG2 ASN D 213 GLY D 225 1 13 HELIX 57 AG3 TRP D 231 VAL D 251 1 21 SHEET 1 AA1 4 GLN I 3 SER I 7 0 SHEET 2 AA1 4 LEU I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AA1 4 GLN I 79 LEU I 84 -1 O LEU I 82 N LEU I 20 SHEET 4 AA1 4 ILE I 71 ASP I 74 -1 N ASP I 74 O GLN I 79 SHEET 1 AA2 6 LEU I 11 VAL I 12 0 SHEET 2 AA2 6 THR I 119 VAL I 123 1 O THR I 122 N VAL I 12 SHEET 3 AA2 6 ALA I 93 VAL I 100 -1 N ALA I 93 O VAL I 121 SHEET 4 AA2 6 GLN I 35 GLN I 41 -1 N ILE I 39 O TYR I 96 SHEET 5 AA2 6 GLU I 48 ILE I 53 -1 O GLU I 48 N ARG I 40 SHEET 6 AA2 6 THR I 59 TYR I 61 -1 O ASN I 60 N ARG I 52 SHEET 1 AA3 4 PHE I 134 LEU I 136 0 SHEET 2 AA3 4 THR I 147 TYR I 157 -1 O LEU I 153 N PHE I 134 SHEET 3 AA3 4 TYR I 188 PRO I 197 -1 O VAL I 194 N LEU I 150 SHEET 4 AA3 4 VAL I 175 THR I 177 -1 N HIS I 176 O VAL I 193 SHEET 1 AA4 4 THR I 143 SER I 144 0 SHEET 2 AA4 4 THR I 147 TYR I 157 -1 O THR I 147 N SER I 144 SHEET 3 AA4 4 TYR I 188 PRO I 197 -1 O VAL I 194 N LEU I 150 SHEET 4 AA4 4 VAL I 181 LEU I 182 -1 N VAL I 181 O SER I 189 SHEET 1 AA5 3 THR I 163 TRP I 166 0 SHEET 2 AA5 3 ILE I 207 HIS I 212 -1 O ASN I 209 N SER I 165 SHEET 3 AA5 3 THR I 217 LYS I 222 -1 O VAL I 219 N VAL I 210 SHEET 1 AA6 4 LEU J 4 SER J 7 0 SHEET 2 AA6 4 ALA J 19 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AA6 4 ASP J 71 ILE J 76 -1 O LEU J 74 N LEU J 21 SHEET 4 AA6 4 PHE J 63 SER J 68 -1 N SER J 64 O THR J 75 SHEET 1 AA7 2 THR J 10 LEU J 13 0 SHEET 2 AA7 2 LYS J 104 ILE J 107 1 O LYS J 104 N LEU J 11 SHEET 1 AA8 5 ASN J 54 ARG J 55 0 SHEET 2 AA8 5 LEU J 47 TYR J 50 -1 N TYR J 50 O ASN J 54 SHEET 3 AA8 5 VAL J 34 GLN J 39 -1 N TRP J 36 O LEU J 48 SHEET 4 AA8 5 VAL J 86 GLN J 91 -1 O GLN J 90 N ALA J 35 SHEET 5 AA8 5 THR J 98 PHE J 99 -1 O THR J 98 N GLN J 91 SHEET 1 AA9 4 SER J 115 PHE J 119 0 SHEET 2 AA9 4 THR J 130 ASN J 138 -1 O LEU J 136 N PHE J 117 SHEET 3 AA9 4 LEU J 176 SER J 183 -1 O LEU J 180 N VAL J 133 SHEET 4 AA9 4 SER J 160 VAL J 164 -1 N GLN J 161 O THR J 179 SHEET 1 AB1 4 ALA J 154 GLN J 156 0 SHEET 2 AB1 4 LYS J 146 VAL J 151 -1 N VAL J 151 O ALA J 154 SHEET 3 AB1 4 VAL J 192 THR J 198 -1 O ALA J 194 N LYS J 150 SHEET 4 AB1 4 VAL J 206 ASN J 211 -1 O LYS J 208 N CYS J 195 SHEET 1 AB2 4 GLN K 3 SER K 7 0 SHEET 2 AB2 4 LEU K 18 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AB2 4 GLN K 79 LEU K 84 -1 O LEU K 84 N LEU K 18 SHEET 4 AB2 4 ILE K 71 ASP K 74 -1 N ASP K 74 O GLN K 79 SHEET 1 AB3 6 LEU K 11 VAL K 12 0 SHEET 2 AB3 6 THR K 119 VAL K 123 1 O THR K 122 N VAL K 12 SHEET 3 AB3 6 ALA K 93 VAL K 100 -1 N ALA K 93 O VAL K 121 SHEET 4 AB3 6 GLN K 35 GLN K 41 -1 N ILE K 39 O TYR K 96 SHEET 5 AB3 6 GLU K 48 ILE K 53 -1 O GLU K 48 N ARG K 40 SHEET 6 AB3 6 THR K 59 TYR K 61 -1 O ASN K 60 N ARG K 52 SHEET 1 AB4 4 PHE K 134 LEU K 136 0 SHEET 2 AB4 4 THR K 147 TYR K 157 -1 O LEU K 153 N PHE K 134 SHEET 3 AB4 4 TYR K 188 PRO K 197 -1 O VAL K 194 N LEU K 150 SHEET 4 AB4 4 VAL K 175 THR K 177 -1 N HIS K 176 O VAL K 193 SHEET 1 AB5 4 THR K 143 SER K 144 0 SHEET 2 AB5 4 THR K 147 TYR K 157 -1 O THR K 147 N SER K 144 SHEET 3 AB5 4 TYR K 188 PRO K 197 -1 O VAL K 194 N LEU K 150 SHEET 4 AB5 4 VAL K 181 LEU K 182 -1 N VAL K 181 O SER K 189 SHEET 1 AB6 3 THR K 163 TRP K 166 0 SHEET 2 AB6 3 ILE K 207 HIS K 212 -1 O ASN K 209 N SER K 165 SHEET 3 AB6 3 THR K 217 LYS K 222 -1 O LYS K 221 N CYS K 208 SHEET 1 AB7 4 LEU L 4 SER L 7 0 SHEET 2 AB7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB7 4 ASP L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AB7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AB8 2 THR L 10 LEU L 13 0 SHEET 2 AB8 2 LYS L 104 ILE L 107 1 O GLU L 106 N LEU L 11 SHEET 1 AB9 5 ASN L 54 ARG L 55 0 SHEET 2 AB9 5 LEU L 47 TYR L 50 -1 N TYR L 50 O ASN L 54 SHEET 3 AB9 5 VAL L 34 GLN L 39 -1 N TRP L 36 O LEU L 48 SHEET 4 AB9 5 VAL L 86 GLN L 91 -1 O TYR L 88 N TYR L 37 SHEET 5 AB9 5 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AC1 4 SER L 115 PHE L 119 0 SHEET 2 AC1 4 THR L 130 ASN L 138 -1 O LEU L 136 N PHE L 117 SHEET 3 AC1 4 LEU L 176 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AC1 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AC2 4 ALA L 154 GLN L 156 0 SHEET 2 AC2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AC2 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AC2 4 VAL L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SHEET 1 AC3 4 GLN M 3 SER M 7 0 SHEET 2 AC3 4 LEU M 18 SER M 25 -1 O SER M 25 N GLN M 3 SHEET 3 AC3 4 GLN M 79 LEU M 84 -1 O LEU M 84 N LEU M 18 SHEET 4 AC3 4 ILE M 71 ASP M 74 -1 N ASP M 74 O GLN M 79 SHEET 1 AC4 6 LEU M 11 VAL M 12 0 SHEET 2 AC4 6 THR M 119 VAL M 123 1 O THR M 122 N VAL M 12 SHEET 3 AC4 6 ALA M 93 VAL M 100 -1 N ALA M 93 O VAL M 121 SHEET 4 AC4 6 GLN M 35 GLN M 41 -1 N ILE M 39 O TYR M 96 SHEET 5 AC4 6 GLU M 48 ILE M 53 -1 O GLU M 48 N ARG M 40 SHEET 6 AC4 6 THR M 59 TYR M 61 -1 O ASN M 60 N ARG M 52 SHEET 1 AC5 4 PHE M 134 LEU M 136 0 SHEET 2 AC5 4 THR M 147 TYR M 157 -1 O LEU M 153 N PHE M 134 SHEET 3 AC5 4 TYR M 188 PRO M 197 -1 O VAL M 194 N LEU M 150 SHEET 4 AC5 4 VAL M 175 THR M 177 -1 N HIS M 176 O VAL M 193 SHEET 1 AC6 4 THR M 143 SER M 144 0 SHEET 2 AC6 4 THR M 147 TYR M 157 -1 O THR M 147 N SER M 144 SHEET 3 AC6 4 TYR M 188 PRO M 197 -1 O VAL M 194 N LEU M 150 SHEET 4 AC6 4 VAL M 181 LEU M 182 -1 N VAL M 181 O SER M 189 SHEET 1 AC7 3 THR M 163 TRP M 166 0 SHEET 2 AC7 3 ILE M 207 HIS M 212 -1 O ASN M 209 N SER M 165 SHEET 3 AC7 3 THR M 217 LYS M 222 -1 O VAL M 219 N VAL M 210 SHEET 1 AC8 4 LEU N 4 SER N 7 0 SHEET 2 AC8 4 ALA N 19 ALA N 25 -1 O ARG N 24 N THR N 5 SHEET 3 AC8 4 ASP N 71 ILE N 76 -1 O LEU N 74 N LEU N 21 SHEET 4 AC8 4 PHE N 63 SER N 68 -1 N SER N 66 O THR N 73 SHEET 1 AC9 2 THR N 10 LEU N 13 0 SHEET 2 AC9 2 LYS N 104 ILE N 107 1 O LYS N 104 N LEU N 11 SHEET 1 AD1 5 ASN N 54 ARG N 55 0 SHEET 2 AD1 5 LEU N 47 TYR N 50 -1 N TYR N 50 O ASN N 54 SHEET 3 AD1 5 VAL N 34 GLN N 39 -1 N TRP N 36 O LEU N 48 SHEET 4 AD1 5 VAL N 86 GLN N 91 -1 O GLN N 90 N ALA N 35 SHEET 5 AD1 5 THR N 98 PHE N 99 -1 O THR N 98 N GLN N 91 SHEET 1 AD2 4 SER N 115 PHE N 119 0 SHEET 2 AD2 4 THR N 130 ASN N 138 -1 O LEU N 136 N PHE N 117 SHEET 3 AD2 4 LEU N 176 SER N 183 -1 O LEU N 180 N VAL N 133 SHEET 4 AD2 4 SER N 160 VAL N 164 -1 N GLN N 161 O THR N 179 SHEET 1 AD3 4 ALA N 154 GLN N 156 0 SHEET 2 AD3 4 LYS N 146 VAL N 151 -1 N VAL N 151 O ALA N 154 SHEET 3 AD3 4 VAL N 192 THR N 198 -1 O ALA N 194 N LYS N 150 SHEET 4 AD3 4 VAL N 206 ASN N 211 -1 O LYS N 208 N CYS N 195 SSBOND 1 CYS I 22 CYS I 97 1555 1555 2.04 SSBOND 2 CYS I 152 CYS I 208 1555 1555 2.04 SSBOND 3 CYS J 23 CYS J 89 1555 1555 2.03 SSBOND 4 CYS J 135 CYS J 195 1555 1555 2.03 SSBOND 5 CYS K 22 CYS K 97 1555 1555 2.04 SSBOND 6 CYS K 152 CYS K 208 1555 1555 2.04 SSBOND 7 CYS L 23 CYS L 89 1555 1555 2.04 SSBOND 8 CYS L 135 CYS L 195 1555 1555 2.03 SSBOND 9 CYS M 22 CYS M 97 1555 1555 2.04 SSBOND 10 CYS M 152 CYS M 208 1555 1555 2.04 SSBOND 11 CYS N 23 CYS N 89 1555 1555 2.04 SSBOND 12 CYS N 135 CYS N 195 1555 1555 2.04 CISPEP 1 ASP I 113 PRO I 114 0 -5.94 CISPEP 2 PHE I 158 PRO I 159 0 -3.67 CISPEP 3 GLU I 160 PRO I 161 0 -1.98 CISPEP 4 SER J 7 PRO J 8 0 -4.54 CISPEP 5 SER J 95 PRO J 96 0 -2.65 CISPEP 6 TYR J 141 PRO J 142 0 0.31 CISPEP 7 ASP K 113 PRO K 114 0 -6.88 CISPEP 8 PHE K 158 PRO K 159 0 -3.62 CISPEP 9 GLU K 160 PRO K 161 0 0.25 CISPEP 10 SER L 7 PRO L 8 0 -4.86 CISPEP 11 SER L 95 PRO L 96 0 -1.61 CISPEP 12 TYR L 141 PRO L 142 0 -1.29 CISPEP 13 ASP M 113 PRO M 114 0 -5.21 CISPEP 14 PHE M 158 PRO M 159 0 -3.79 CISPEP 15 GLU M 160 PRO M 161 0 -1.07 CISPEP 16 SER N 7 PRO N 8 0 -4.18 CISPEP 17 SER N 95 PRO N 96 0 -1.40 CISPEP 18 TYR N 141 PRO N 142 0 -2.07 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000